GENTAUR Molecular Products.

 CDC73_HUMAN             Reviewed;         531 AA.
 Q6P1J9; A6NLZ8; B2RBR2; Q6PK51; Q96A07; Q9H245; Q9H5L7;
 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
 05-JUL-2004, sequence version 1.
 07-NOV-2018, entry version 158.
 RecName: Full=Parafibromin;
 AltName: Full=Cell division cycle protein 73 homolog;
 AltName: Full=Hyperparathyroidism 2 protein;
 Name=CDC73; Synonyms=C1orf28, HRPT2;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=11318611; DOI=10.1006/geno.2001.6500;
 Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
 Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
 Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
 Carpten J.D.;
 "Cloning and characterization of 13 novel transcripts and the human
 RGS8 gene from the 1q25 region encompassing the hereditary prostate
 cancer (HPC1) locus.";
 Genomics 73:211-222(2001).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16710414; DOI=10.1038/nature04727;
 Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
 Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
 Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
 McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
 Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
 Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
 Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
 Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
 Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
 Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
 Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
 Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
 Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
 Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
 Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
 Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
 Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
 Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
 Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
 Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
 Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
 Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
 Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
 Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
 Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
 Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
 Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
 Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
 Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
 Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
 Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
 Beck S., Rogers J., Bentley D.R.;
 "The DNA sequence and biological annotation of human chromosome 1.";
 Nature 441:315-321(2006).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Eye, and Urinary bladder;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [6]
 PROTEIN SEQUENCE OF 2-9; 38-47; 78-87; 111-120; 127-136; 172-181;
 212-222; 235-243; 248-257; 332-342; 379-385 AND 400-407, CLEAVAGE OF
 INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
 SPECTROMETRY.
 TISSUE=Embryonic kidney, and Ovarian carcinoma;
 Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
 Ramsay A., Leung H.Y.;
 Submitted (FEB-2008) to UniProtKB.
 [7]
 FUNCTION, INTERACTION WITH PAF1; LEO1 AND POLR2A, INTERACTION WITH
 SET1-LIKE COMPLEX, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
 VARIANT HRPT1 PRO-64.
 PubMed=15632063; DOI=10.1128/MCB.25.2.612-620.2005;
 Rozenblatt-Rosen O., Hughes C.M., Nannepaga S.J., Shanmugam K.S.,
 Copeland T.D., Guszczynski T., Resau J.H., Meyerson M.;
 "The parafibromin tumor suppressor protein is part of a human Paf1
 complex.";
 Mol. Cell. Biol. 25:612-620(2005).
 [8]
 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAF1 AND POLR2A.
 PubMed=15923622; DOI=10.1128/MCB.25.12.5052-5060.2005;
 Yart A., Gstaiger M., Wirbelauer C., Pecnik M., Anastasiou D.,
 Hess D., Krek W.;
 "The HRPT2 tumor suppressor gene product parafibromin associates with
 human PAF1 and RNA polymerase II.";
 Mol. Cell. Biol. 25:5052-5060(2005).
 [9]
 FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
 PubMed=15580289; DOI=10.1038/sj.onc.1208274;
 Woodard G.E., Lin L., Zhang J.-H., Agarwal S.K., Marx S.J.,
 Simonds W.F.;
 "Parafibromin, product of the hyperparathyroidism-jaw tumor syndrome
 gene HRPT2, regulates cyclin D1/PRAD1 expression.";
 Oncogene 24:1272-1276(2005).
 [10]
 CHARACTERIZATION OF NUCLEAR LOCALIZATION SIGNAL.
 PubMed=16116486; DOI=10.1038/sj.onc.1208778;
 Hahn M.A., Marsh D.J.;
 "Identification of a functional bipartite nuclear localization signal
 in the tumor suppressor parafibromin.";
 Oncogene 24:6241-6248(2005).
 [11]
 INVOLVEMENT IN HRPT2, INVOLVEMENT IN HRPT1, AND VARIANT HRPT1 PRO-64.
 PubMed=12434154; DOI=10.1038/ng1048;
 Carpten J.D., Robbins C.M., Villablanca A., Forsberg L.,
 Presciuttini S., Bailey-Wilson J., Simonds W.F., Gillanders E.M.,
 Kennedy A.M., Chen J.D., Agarwal S.K., Sood R., Jones M.P.,
 Moses T.Y., Haven C., Petillo D., Leotlela P.D., Harding B.,
 Cameron D., Pannett A.A., Hoeoeg A., Heath H. III, James-Newton L.A.,
 Robinson B., Zarbo R.J., Cavaco B.M., Wassif W., Perrier N.D.,
 Rosen I.B., Kristoffersson U., Turnpenny P.D., Farnebo L.-O.,
 Besser G.M., Jackson C.E., Morreau H., Trent J.M., Thakker R.V.,
 Marx S.J., Teh B.T., Larsson C., Hobbs M.R.;
 "HRPT2, encoding parafibromin, is mutated in hyperparathyroidism-jaw
 tumor syndrome.";
 Nat. Genet. 32:676-680(2002).
 [12]
 INVOLVEMENT IN PRTC.
 PubMed=14585940; DOI=10.1056/NEJMoa031237;
 Shattuck T.M., Vaelimaeki S., Obara T., Gaz R.D., Clark O.H.,
 Shoback D., Wierman M.E., Tojo K., Robbins C.M., Carpten J.D.,
 Farnebo L.-O., Larsson C., Arnold A.;
 "Somatic and germ-line mutations of the HRPT2 gene in sporadic
 parathyroid carcinoma.";
 N. Engl. J. Med. 349:1722-1729(2003).
 [13]
 FUNCTION.
 PubMed=16989776; DOI=10.1016/j.bbrc.2006.08.169;
 Zhang C., Kong D., Tan M.H., Pappas D.L. Jr., Wang P.F., Chen J.,
 Farber L., Zhang N., Koo H.M., Weinreich M., Williams B.O., Teh B.T.;
 "Parafibromin inhibits cancer cell growth and causes G1 phase
 arrest.";
 Biochem. Biophys. Res. Commun. 350:17-24(2006).
 [14]
 FUNCTION, AND INTERACTION WITH CTNNB1.
 PubMed=16630820; DOI=10.1016/j.cell.2006.01.053;
 Mosimann C., Hausmann G., Basler K.;
 "Parafibromin/Hyrax activates Wnt/Wg target gene transcription by
 direct association with beta-catenin/Armadillo.";
 Cell 125:327-341(2006).
 [15]
 IDENTIFICATION IN A COMPLEX WITH BCL9L; CTNNB1 AND PYGO1.
 PubMed=17113272; DOI=10.1016/j.mod.2006.09.006;
 Hoffmans R., Basler K.;
 "BCL9-2 binds Arm/beta-catenin in a Tyr142-independent manner and
 requires Pygopus for its function in Wg/Wnt signaling.";
 Mech. Dev. 124:59-67(2007).
 [16]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18669648; DOI=10.1073/pnas.0805139105;
 Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
 Elledge S.J., Gygi S.P.;
 "A quantitative atlas of mitotic phosphorylation.";
 Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
 [17]
 IDENTIFICATION IN THE PAF1 COMPLEX, AND FUNCTION OF THE PAF1 COMPLEX.
 PubMed=19952111; DOI=10.1101/gad.1834709;
 Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T.,
 Nakamura M., Hisatake K., Handa H.;
 "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative
 roles in RNA polymerase II elongation.";
 Genes Dev. 23:2765-2777(2009).
 [18]
 FUNCTION, AND INTERACTION WITH CPSF1; CPSF4 AND CSTF2.
 PubMed=19136632; DOI=10.1073/pnas.0812023106;
 Rozenblatt-Rosen O., Nagaike T., Francis J.M., Kaneko S., Glatt K.A.,
 Hughes C.M., LaFramboise T., Manley J.L., Meyerson M.;
 "The tumor suppressor Cdc73 functionally associates with CPSF and CstF
 3' mRNA processing factors.";
 Proc. Natl. Acad. Sci. U.S.A. 106:755-760(2009).
 [19]
 FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH KMT2A.
 PubMed=20541477; DOI=10.1016/j.ccr.2010.04.012;
 Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J.,
 Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.;
 "The PAF complex synergizes with MLL fusion proteins at HOX loci to
 promote leukemogenesis.";
 Cancer Cell 17:609-621(2010).
 [20]
 IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
 AND FUNCTION OF THE PAF1 COMPLEX.
 PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
 Kim J., Guermah M., Roeder R.G.;
 "The human PAF1 complex acts in chromatin transcription elongation
 both independently and cooperatively with SII/TFIIS.";
 Cell 140:491-503(2010).
 [21]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=20068231; DOI=10.1126/scisignal.2000475;
 Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
 Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
 Mann M.;
 "Quantitative phosphoproteomics reveals widespread full
 phosphorylation site occupancy during mitosis.";
 Sci. Signal. 3:RA3-RA3(2010).
 [22]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21269460; DOI=10.1186/1752-0509-5-17;
 Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
 Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
 "Initial characterization of the human central proteome.";
 BMC Syst. Biol. 5:17-17(2011).
 [23]
 FUNCTION, AND FUNCTION OF THE PAF1 COMPLEX.
 PubMed=21329879; DOI=10.1016/j.molcel.2011.01.022;
 Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M.,
 Manley J.L.;
 "Transcriptional activators enhance polyadenylation of mRNA
 precursors.";
 Mol. Cell 41:409-418(2011).
 [24]
 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
 METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
 SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=22223895; DOI=10.1074/mcp.M111.015131;
 Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
 Meinnel T., Giglione C.;
 "Comparative large-scale characterisation of plant vs. mammal proteins
 reveals similar and idiosyncratic N-alpha acetylation features.";
 Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
 [25]
 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
 METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
 SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=22814378; DOI=10.1073/pnas.1210303109;
 Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
 Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
 Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
 Aldabe R.;
 "N-terminal acetylome analyses and functional insights of the N-
 terminal acetyltransferase NatB.";
 Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
 [26]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [27]
 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-301, AND IDENTIFICATION BY
 MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=25218447; DOI=10.1038/nsmb.2890;
 Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
 Vertegaal A.C.;
 "Uncovering global SUMOylation signaling networks in a site-specific
 manner.";
 Nat. Struct. Mol. Biol. 21:927-936(2014).
 [28]
 INTERACTION WITH PTPN11, DEPHOSPHORYLATION BY PTPN11, AND
 PHOSPHORYLATION.
 PubMed=26742426; DOI=10.1016/j.bbrc.2015.12.117;
 Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.;
 "Determination of the catalytic activity of LEOPARD syndrome-
 associated SHP2 mutants toward parafibromin, a bona fide SHP2
 substrate involved in Wnt signaling.";
 Biochem. Biophys. Res. Commun. 469:1133-1139(2016).
 [29]
 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-198; LYS-301; LYS-308 AND
 LYS-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 PubMed=28112733; DOI=10.1038/nsmb.3366;
 Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
 Nielsen M.L.;
 "Site-specific mapping of the human SUMO proteome reveals co-
 modification with phosphorylation.";
 Nat. Struct. Mol. Biol. 24:325-336(2017).
 [30]
 VARIANT HRPT1 PRO-64.
 PubMed=12960210; DOI=10.1136/jmg.40.9.657;
 Howell V.M., Haven C.J., Kahnoski K., Khoo S.K., Petillo D., Chen J.,
 Fleuren G.J., Robinson B.G., Delbridge L.W., Philips J., Nelson A.E.,
 Krause U., Hammje K., Dralle H., Hoang-Vu C., Gimm O., Marsh D.J.,
 Morreau H., Teh B.T.;
 "HRPT2 mutations are associated with malignancy in sporadic
 parathyroid tumours.";
 J. Med. Genet. 40:657-663(2003).
 [31]
 VARIANT HRPT2 5-LEU--GLN-10 DEL, AND INVOLVEMENT IN HRPT2.
 PubMed=15613436; DOI=10.1210/jc.2004-0991;
 Moon S.D., Park J.H., Kim E.M., Kim J.H., Han J.H., Yoo S.J.,
 Yoon K.H., Kang M.I., Lee K.W., Son H.Y., Kang S.K., Oh S.J.,
 Kim K.M., Yoon S.J., Park J.G., Kim I.J., Kang H.C., Hong S.W.,
 Kim K.R., Cha B.Y.;
 "A Novel IVS2-1G>A mutation causes aberrant splicing of the HRPT2 gene
 in a family with hyperparathyroidism-jaw tumor syndrome.";
 J. Clin. Endocrinol. Metab. 90:878-883(2005).
 [32]
 VARIANT HRPT2 ASN-379, VARIANT HRPT1 PRO-95, AND INVOLVEMENT IN HRPT1.
 PubMed=16487440; DOI=10.1111/j.1365-2265.2006.02460.x;
 Bradley K.J., Cavaco B.M., Bowl M.R., Harding B., Cranston T.,
 Fratter C., Besser G.M., Conceicao Pereira M., Davie M.W., Dudley N.,
 Leite V., Sadler G.P., Seller A., Thakker R.V.;
 "Parafibromin mutations in hereditary hyperparathyroidism syndromes
 and parathyroid tumours.";
 Clin. Endocrinol. (Oxf.) 64:299-306(2006).
 [33]
 VARIANT SER-272, AND ASSOCIATION WITH PARATHYROID ADENOMA.
 PubMed=16728578; DOI=10.1677/erc.1.01058;
 Juhlin C., Larsson C., Yakoleva T., Leibiger I., Leibiger B.,
 Alimov A., Weber G., Hoog A., Villablanca A.;
 "Loss of parafibromin expression in a subset of parathyroid
 adenomas.";
 Endocr. Relat. Cancer 13:509-523(2006).
 [34]
 VARIANT PHE-59, AND ASSOCIATION WITH PARATHYROID CARCINOMA.
 PubMed=17555500; DOI=10.1111/j.1365-2265.2007.02894.x;
 Haven C.J., van Puijenbroek M., Tan M.H., Teh B.T., Fleuren G.J.,
 van Wezel T., Morreau H.;
 "Identification of MEN1 and HRPT2 somatic mutations in paraffin-
 embedded (sporadic) parathyroid carcinomas.";
 Clin. Endocrinol. (Oxf.) 67:370-376(2007).
 [35]
 VARIANTS SER-2 AND PRO-91, AND ASSOCIATION WITH PARATHYROID ADENOMA.
 PubMed=17639062; DOI=10.1677/ERC-06-0092;
 Cetani F., Pardi E., Ambrogini E., Viacava P., Borsari S., Lemmi M.,
 Cianferotti L., Miccoli P., Pinchera A., Arnold A., Marcocci C.;
 "Different somatic alterations of the HRPT2 gene in a patient with
 recurrent sporadic primary hyperparathyroidism carrying an HRPT2
 germline mutation.";
 Endocr. Relat. Cancer 14:493-499(2007).
 [36]
 VARIANTS GLN-34 AND LYS-292, CHARACTERIZATION OF VARIANT GLN-34, AND
 ASSOCIATION WITH RENAL TUMORS.
 PubMed=17130827; DOI=10.1038/sj.onc.1210131;
 Zhao J., Yart A., Frigerio S., Perren A., Schraml P., Weisstanner C.,
 Stallmach T., Krek W., Moch H.;
 "Sporadic human renal tumors display frequent allelic imbalances and
 novel mutations of the HRPT2 gene.";
 Oncogene 26:3440-3449(2007).
 [37]
 VARIANT HRPT1 PRO-63, AND INVOLVEMENT IN HRPT1.
 PubMed=18755853; DOI=10.1677/ERC-08-0066;
 Masi G., Barzon L., Iacobone M., Viel G., Porzionato A., Macchi V.,
 De Caro R., Favia G., Palu G.;
 "Clinical, genetic, and histopathologic investigation of CDC73-related
 familial hyperparathyroidism.";
 Endocr. Relat. Cancer 15:1115-1126(2008).
 -!- FUNCTION: Tumor suppressor probably involved in transcriptional
     and post-transcriptional control pathways. May be involved in cell
     cycle progression through the regulation of cyclin D1/PRAD1
     expression. Component of the PAF1 complex (PAF1C) which has
     multiple functions during transcription by RNA polymerase II and
     is implicated in regulation of development and maintenance of
     embryonic stem cell pluripotency. PAF1C associates with RNA
     polymerase II through interaction with POLR2A CTD non-
     phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
     is involved in transcriptional elongation, acting both
     indepentently and synergistically with TCEA1 and in cooperation
     with the DSIF complex and HTATSF1. PAF1C is required for
     transcription of Hox and Wnt target genes. PAF1C is involved in
     hematopoiesis and stimulates transcriptional activity of
     KMT2A/MLL1; it promotes leukemogenesis through association with
     KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9
     and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone
     modifications such as ubiquitination of histone H2B and
     methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the
     RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme
     UBE2A or UBE2B to chromatin which mediate monoubiquitination of
     'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
     ubiquitination is proposed to be coupled to transcription. PAF1C
     is involved in mRNA 3' end formation probably through association
     with cleavage and poly(A) factors. In case of infection by
     influenza A strain H3N2, PAF1C associates with viral NS1 protein,
     thereby regulating gene transcription. Connects PAF1C with the
     cleavage and polyadenylation specificity factor (CPSF) complex and
     the cleavage stimulation factor (CSTF) complex, and with Wnt
     signaling. Involved in polyadenylation of mRNA precursors.
     {ECO:0000269|PubMed:15580289, ECO:0000269|PubMed:15632063,
     ECO:0000269|PubMed:15923622, ECO:0000269|PubMed:16630820,
     ECO:0000269|PubMed:16989776, ECO:0000269|PubMed:19136632,
     ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
     ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879}.
 -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
     PAF1, LEO1, CTR9, RTF1 and WDR61 (PubMed:19952111,
     PubMed:20178742). The PAF1 complex interacts with PHF5A. Within
     the PAF1 complex interacts directly with PHF5A (By similarity).
     Interacts with POLR2A, CPSF1, CPSF4, CSTF2, KMT2A/MLL1 and CTNNB1
     (PubMed:15632063, PubMed:15923622, PubMed:16630820,
     PubMed:19136632, PubMed:20541477). Interacts with a Set1-like
     complex that has histone methyltransferase activity and methylates
     histone H3 (PubMed:15632063). Found in a complex with BCL9L or
     BCL9, CDC73, CTNNB1 and PYGO1 indicative for the participation in
     a nuclear Wnt signaling complex (PubMed:17113272). Interacts with
     PTPN11 (PubMed:26742426). Interacts with SETD5 (By similarity).
     {ECO:0000250|UniProtKB:Q8JZM7, ECO:0000269|PubMed:15632063,
     ECO:0000269|PubMed:15923622, ECO:0000269|PubMed:16630820,
     ECO:0000269|PubMed:17113272, ECO:0000269|PubMed:19136632,
     ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
     ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:26742426}.
 -!- INTERACTION:
     P13196:ALAS1; NbExp=8; IntAct=EBI-930143, EBI-3905054;
     O00512:BCL9; NbExp=2; IntAct=EBI-930143, EBI-533127;
     Q8N6L0:CCDC155; NbExp=6; IntAct=EBI-930143, EBI-749265;
     Q8NHQ1:CEP70; NbExp=9; IntAct=EBI-930143, EBI-739624;
     O95639:CPSF4; NbExp=3; IntAct=EBI-930143, EBI-725860;
     P33240:CSTF2; NbExp=5; IntAct=EBI-930143, EBI-711360;
     P35222:CTNNB1; NbExp=9; IntAct=EBI-930143, EBI-491549;
     Q6PD62:CTR9; NbExp=19; IntAct=EBI-930143, EBI-1019583;
     A1L4K1:FSD2; NbExp=8; IntAct=EBI-930143, EBI-5661036;
     Q08379:GOLGA2; NbExp=10; IntAct=EBI-930143, EBI-618309;
     O75031:HSF2BP; NbExp=3; IntAct=EBI-930143, EBI-7116203;
     Q03164:KMT2A; NbExp=4; IntAct=EBI-930143, EBI-591370;
     Q8WVC0:LEO1; NbExp=15; IntAct=EBI-930143, EBI-932432;
     Q5JR59:MTUS2; NbExp=5; IntAct=EBI-930143, EBI-742948;
     Q5JR59-3:MTUS2; NbExp=5; IntAct=EBI-930143, EBI-11522433;
     Q8N7H5:PAF1; NbExp=27; IntAct=EBI-930143, EBI-2607770;
     P24928:POLR2A; NbExp=6; IntAct=EBI-930143, EBI-295301;
     Q92541:RTF1; NbExp=12; IntAct=EBI-930143, EBI-1055239;
     Q12800:TFCP2; NbExp=8; IntAct=EBI-930143, EBI-717422;
     Q9BZW7:TSGA10; NbExp=8; IntAct=EBI-930143, EBI-744794;
     Q9H9H4:VPS37B; NbExp=3; IntAct=EBI-930143, EBI-4400866;
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15580289,
     ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15923622}.
 -!- TISSUE SPECIFICITY: Found in adrenal and parathyroid glands,
     kidney and heart. {ECO:0000269|PubMed:15580289}.
 -!- PTM: Phosphorylated. Dephosphorylated by PTPN11.
     {ECO:0000269|PubMed:26742426}.
 -!- DISEASE: Hyperparathyroidism 1 (HRPT1) [MIM:145000]: An autosomal
     dominant disorder characterized by hypercalcemia, elevated
     parathyroid hormone (PTH) levels, and uniglandular or
     multiglandular parathyroid hyperplasia, adenomas, and carcinomas.
     {ECO:0000269|PubMed:12434154, ECO:0000269|PubMed:12960210,
     ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:16487440,
     ECO:0000269|PubMed:18755853}. Note=The disease is caused by
     mutations affecting the gene represented in this entry.
 -!- DISEASE: Hyperparathyroidism 2 with jaw tumors (HRPT2)
     [MIM:145001]: An autosomal dominant neoplasia syndrome
     characterized by primary hyperparathyroidism, ossifying fibroma of
     the maxilla and/or mandible, renal tumor, and uterine tumors. It
     is associated with increased risk of parathyroid cancer.
     {ECO:0000269|PubMed:12434154, ECO:0000269|PubMed:15613436,
     ECO:0000269|PubMed:16487440}. Note=The disease is caused by
     mutations affecting the gene represented in this entry.
 -!- DISEASE: Parathyroid carcinoma (PRTC) [MIM:608266]: These cancers
     characteristically result in more profound clinical manifestations
     of hyperparathyroidism than do parathyroid adenomas, the most
     frequent cause of primary hyperparathyroidism. Early en bloc
     resection of the primary tumor is the only curative treatment.
     {ECO:0000269|PubMed:14585940}. Note=The gene represented in this
     entry is involved in disease pathogenesis.
 -!- SIMILARITY: Belongs to the CDC73 family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAH07325.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 300.; Evidence={ECO:0000305};
     Sequence=BAB15608.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
     and Haematology;
     URL="http://atlasgeneticsoncology.org/Genes/CDC73ID181ch1q31.html";
 -----------------------------------------------------------------------
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 Distributed under the Creative Commons Attribution (CC BY 4.0) License
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 EMBL; AF312865; AAG45339.1; -; mRNA.
 EMBL; AK026969; BAB15608.1; ALT_INIT; mRNA.
 EMBL; AK314772; BAG37309.1; -; mRNA.
 EMBL; AL139133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AL390863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471067; EAW91250.1; -; Genomic_DNA.
 EMBL; BC007325; AAH07325.1; ALT_SEQ; mRNA.
 EMBL; BC014351; AAH14351.2; -; mRNA.
 EMBL; BC065037; AAH65037.1; -; mRNA.
 CCDS; CCDS1382.1; -.
 RefSeq; NP_078805.3; NM_024529.4.
 UniGene; Hs.378996; -.
 PDB; 5YDE; X-ray; 1.02 A; A=1-111.
 PDB; 5YDF; X-ray; 1.40 A; A/B=1-100.
 PDBsum; 5YDE; -.
 PDBsum; 5YDF; -.
 ProteinModelPortal; Q6P1J9; -.
 SMR; Q6P1J9; -.
 BioGrid; 122724; 265.
 CORUM; Q6P1J9; -.
 DIP; DIP-37884N; -.
 IntAct; Q6P1J9; 98.
 MINT; Q6P1J9; -.
 STRING; 9606.ENSP00000356405; -.
 iPTMnet; Q6P1J9; -.
 PhosphoSitePlus; Q6P1J9; -.
 BioMuta; CDC73; -.
 DMDM; 74749063; -.
 EPD; Q6P1J9; -.
 MaxQB; Q6P1J9; -.
 PaxDb; Q6P1J9; -.
 PeptideAtlas; Q6P1J9; -.
 PRIDE; Q6P1J9; -.
 ProteomicsDB; 66834; -.
 DNASU; 79577; -.
 Ensembl; ENST00000367435; ENSP00000356405; ENSG00000134371.
 GeneID; 79577; -.
 KEGG; hsa:79577; -.
 UCSC; uc001gtb.4; human.
 CTD; 79577; -.
 DisGeNET; 79577; -.
 EuPathDB; HostDB:ENSG00000134371.9; -.
 GeneCards; CDC73; -.
 GeneReviews; CDC73; -.
 HGNC; HGNC:16783; CDC73.
 HPA; CAB016359; -.
 HPA; HPA030772; -.
 MalaCards; CDC73; -.
 MIM; 145000; phenotype.
 MIM; 145001; phenotype.
 MIM; 607393; gene.
 MIM; 608266; phenotype.
 neXtProt; NX_Q6P1J9; -.
 OpenTargets; ENSG00000134371; -.
 Orphanet; 99879; Familial isolated hyperparathyroidism.
 Orphanet; 99880; Hyperparathyroidism-jaw tumor syndrome.
 Orphanet; 143; Parathyroid carcinoma.
 PharmGKB; PA29464; -.
 eggNOG; KOG3786; Eukaryota.
 eggNOG; COG5157; LUCA.
 GeneTree; ENSGT00390000001114; -.
 HOVERGEN; HBG055033; -.
 InParanoid; Q6P1J9; -.
 KO; K15175; -.
 OMA; KKLQGCQ; -.
 OrthoDB; EOG091G0A8X; -.
 PhylomeDB; Q6P1J9; -.
 TreeFam; TF313016; -.
 Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
 Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
 Reactome; R-HSA-5632684; Hedgehog 'on' state.
 Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
 Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
 Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
 SignaLink; Q6P1J9; -.
 SIGNOR; Q6P1J9; -.
 ChiTaRS; CDC73; human.
 GeneWiki; CDC73; -.
 GenomeRNAi; 79577; -.
 PRO; PR:Q6P1J9; -.
 Proteomes; UP000005640; Chromosome 1.
 Bgee; ENSG00000134371; Expressed in 206 organ(s), highest expression level in brain.
 CleanEx; HS_CDC73; -.
 ExpressionAtlas; Q6P1J9; baseline and differential.
 Genevisible; Q6P1J9; HS.
 GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
 GO; GO:0005829; C:cytosol; IDA:HPA.
 GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
 GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO; GO:0005634; C:nucleus; IDA:UniProtKB.
 GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
 GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
 GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
 GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
 GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
 GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
 GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
 GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
 GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:UniProtKB.
 GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
 GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
 GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
 GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
 GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
 GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
 GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
 GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
 GO; GO:0034402; P:recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex; IBA:GO_Central.
 GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
 GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
 GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
 Gene3D; 3.40.50.11990; -; 1.
 InterPro; IPR007852; Cdc73/Parafibromin.
 InterPro; IPR031336; CDC73_C.
 InterPro; IPR038103; CDC73_C_sf.
 InterPro; IPR032041; Cdc73_N.
 PANTHER; PTHR12466; PTHR12466; 1.
 Pfam; PF05179; CDC73_C; 1.
 Pfam; PF16050; CDC73_N; 1.
 1: Evidence at protein level;
 3D-structure; Acetylation; Cell cycle; Complete proteome;
 Direct protein sequencing; Disease mutation; Isopeptide bond; Nucleus;
 Phosphoprotein; Reference proteome; Transcription;
 Transcription regulation; Tumor suppressor; Ubl conjugation;
 Wnt signaling pathway.
 INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895,
                              ECO:0000244|PubMed:22814378,
                              ECO:0000269|Ref.6}.
 CHAIN         2    531       Parafibromin.
                              /FTId=PRO_0000191803.
 REGION      200    531       Interaction with POLR2A and PAF1.
 REGION      200    250       Interaction with CTNNB1.
                              {ECO:0000269|PubMed:16630820}.
 MOTIF       125    139       Nuclear localization signal.
 COMPBIAS    361    364       Poly-Ile.
 MOD_RES       2      2       N-acetylalanine.
                              {ECO:0000244|PubMed:22223895,
                              ECO:0000244|PubMed:22814378,
                              ECO:0000269|Ref.6}.
 MOD_RES     212    212       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 CROSSLNK    198    198       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    301    301       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:25218447,
                              ECO:0000244|PubMed:28112733}.
 CROSSLNK    308    308       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    321    321       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 VARIANT       2      2       A -> S (found in parathyroid adenoma
                              samples; somatic mutation; parathyroid
                              adenoma samples are from a patient with
                              isolated hyperparathyroidism who also
                              carries germline mutation P-91).
                              {ECO:0000269|PubMed:17639062}.
                              /FTId=VAR_064927.
 VARIANT       5     10       Missing (in HRPT2; unknown pathological
                              significance; found as somatic mutation
                              in a parathyroid carcinoma sample from a
                              patient who also carries a germline
                              mutation causing a splicing defect).
                              {ECO:0000269|PubMed:15613436}.
                              /FTId=VAR_064928.
 VARIANT      34     34       K -> Q (found in a clear cell renal
                              carcinoma sample; somatic mutation;
                              unlike wild-type protein the mutant is
                              defective in suppressing CCND1 expression
                              in vivo). {ECO:0000269|PubMed:17130827}.
                              /FTId=VAR_064929.
 VARIANT      59     59       S -> F (found in a parathyroid carcinoma
                              sample; somatic mutation).
                              {ECO:0000269|PubMed:17555500}.
                              /FTId=VAR_064930.
 VARIANT      63     63       L -> P (in HRPT1; unknown pathological
                              significance; dbSNP:rs1060500015).
                              {ECO:0000269|PubMed:18755853}.
                              /FTId=VAR_064931.
 VARIANT      64     64       L -> P (in HRPT1; does not affect
                              interaction with the Pfa1 complex;
                              dbSNP:rs121434264).
                              {ECO:0000269|PubMed:12434154,
                              ECO:0000269|PubMed:12960210,
                              ECO:0000269|PubMed:15632063}.
                              /FTId=VAR_024082.
 VARIANT      91     91       R -> P (found in a patient with isolated
                              hyperparathyroidism and parathyroid
                              adenomas). {ECO:0000269|PubMed:17639062}.
                              /FTId=VAR_064932.
 VARIANT      95     95       L -> P (in HRPT1; unknown pathological
                              significance; found as somatic mutation
                              in a parathyroid adenoma sample from a
                              patient who also carries a germline
                              frameshift mutation).
                              {ECO:0000269|PubMed:16487440}.
                              /FTId=VAR_064933.
 VARIANT     272    272       N -> S (found in a parathyroid adenoma
                              sample; dbSNP:rs752383339).
                              {ECO:0000269|PubMed:16728578}.
                              /FTId=VAR_064934.
 VARIANT     292    292       R -> K (found in a Wilms tumor sample;
                              somatic mutation).
                              {ECO:0000269|PubMed:17130827}.
                              /FTId=VAR_064935.
 VARIANT     379    379       D -> N (in HRPT2; dbSNP:rs971586985).
                              {ECO:0000269|PubMed:16487440}.
                              /FTId=VAR_064936.
 VARIANT     384    384       L -> P (in dbSNP:rs35590728).
                              /FTId=VAR_031825.
 CONFLICT    123    123       Q -> G (in Ref. 5; AAH14351).
                              {ECO:0000305}.
 CONFLICT    184    187       AIKA -> CNQT (in Ref. 2; BAB15608).
                              {ECO:0000305}.
 CONFLICT    372    372       I -> K (in Ref. 2; BAB15608).
                              {ECO:0000305}.
 HELIX         4     14       {ECO:0000244|PDB:5YDE}.
 STRAND       19     21       {ECO:0000244|PDB:5YDE}.
 STRAND       24     27       {ECO:0000244|PDB:5YDE}.
 STRAND       30     33       {ECO:0000244|PDB:5YDE}.
 STRAND       37     41       {ECO:0000244|PDB:5YDE}.
 STRAND       54     56       {ECO:0000244|PDB:5YDE}.
 HELIX        57     65       {ECO:0000244|PDB:5YDE}.
 TURN         66     68       {ECO:0000244|PDB:5YDE}.
 HELIX        71     81       {ECO:0000244|PDB:5YDE}.
 HELIX        88     98       {ECO:0000244|PDB:5YDE}.
 SEQUENCE   531 AA;  60577 MW;  894A7448DBC0E793 CRC64;
 MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ PREYYTLDSI
 LFLLNNVHLS HPVYVRRAAT ENIPVVRRPD RKDLLGYLNG EASTSASIDR SAPLEIGLQR
 STQVKRAADE VLAEAKKPRI EDEECVRLDK ERLAARLEGH KEGIVQTEQI RSLSEAMSVE
 KIAAIKAKIM AKKRSTIKTD LDDDITALKQ RSFVDAEVDV TRDIVSRERV WRTRTTILQS
 TGKNFSKNIF AILQSVKARE EGRAPEQRPA PNAAPVDPTL RTKQPIPAAY NRYDQERFKG
 KEETEGFKID TMGTYHGMTL KSVTEGASAR KTQTPAAQPV PRPVSQARPP PNQKKGSRTP
 IIIIPAATTS LITMLNAKDL LQDLKFVPSD EKKKQGCQRE NETLIQRRKD QMQPGGTAIS
 VTVPYRVVDQ PLKLMPQDWD RVVAVFVQGP AWQFKGWPWL LPDGSPVDIF AKIKAFHLKY
 DEVRLDPNVQ KWDVTVLELS YHKRHLDRPV FLRFWETLDR YMVKHKSHLR F

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